Improving the Secretory Production of the Heterologous Protein in Pichia pastoris by Focusing on Protein Folding

被引：27

作者：

Yu, Ping ^{[1
]}

Zhu, Qi ^{[1
]}

Chen, Kaifei ^{[1
]}

Lv, Xiuhong ^{[1
]}

机构：

[1] Zhejiang Gongshang Univ, Coll Food Sci & Biotechnol, Hangzhou 310035, Zhejiang, Peoples R China

来源：

APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY | 2015年 / 175卷 / 01期

基金：

中国国家自然科学基金;

关键词：

Protein folding; Heterologous protein; P; pastoris; Secretory production; LINKED OLIGOSACCHARIDE STRUCTURES; YEAST SACCHAROMYCES-CEREVISIAE; HIGH-LEVEL EXPRESSION; HUMAN SERUM-ALBUMIN; ENDOPLASMIC-RETICULUM; METHYLOTROPHIC YEAST; QUALITY-CONTROL; RECOMBINANT PROTEINS; MOLECULAR CHAPERONES; BIOLOGICAL-ACTIVITY;

D O I：

10.1007/s12010-014-1292-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Pichia pastoris has currently been developed as an effective host system for the expression of heterologous genes owing to its potential use for the production of soluble and high-yield proteins. However, the secretory production of the different heterologous proteins in P. pastoris varies widely. Some factors restrict the effective secretory production of heterologous proteins in P. pastoris, among which the folding and processing of proteins is a major one. Besides optimizing the fermentative process, current strategies focus on investigating protein folding process. Thus, this paper is the first time to review the improvement of the secretory production of the heterologous protein in P. pastoris by focusing on its folding process.

引用

页码：535 / 548

页数：14

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